ID   SECA1_MYCTA             Reviewed;         949 AA.
AC   A5U7R4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Protein translocase subunit SecA 1 {ECO:0000255|HAMAP-Rule:MF_01382};
DE            EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN   Name=secA1 {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=MRA_3281;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with
CC       the SecYEG preprotein conducting channel. Has a central role in
CC       coupling the hydrolysis of ATP to the transfer of proteins into and
CC       across the cell membrane, serving as an ATP-driven molecular motor
CC       driving the stepwise translocation of polypeptide chains across the
CC       membrane. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC         cellular proteinSide 2.; EC=7.4.2.8; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01382};
CC   -!- SUBUNIT: Monomer and homodimer. Part of the essential Sec protein
CC       translocation apparatus which comprises SecA, SecYEG and auxiliary
CC       proteins SecDF. Other proteins may also be involved.
CC       {ECO:0000255|HAMAP-Rule:MF_01382}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01382};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382};
CC       Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm
CC       {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50.
CC       {ECO:0000255|HAMAP-Rule:MF_01382}.
CC   -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01382}.
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DR   EMBL; CP000611; ABQ75064.1; -; Genomic_DNA.
DR   RefSeq; WP_003901576.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U7R4; -.
DR   SMR; A5U7R4; -.
DR   STRING; 419947.MRA_3281; -.
DR   EnsemblBacteria; ABQ75064; ABQ75064; MRA_3281.
DR   GeneID; 45427234; -.
DR   KEGG; mra:MRA_3281; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_0_11; -.
DR   OMA; MVHYDVQ; -.
DR   OrthoDB; 212453at2; -.
DR   Proteomes; UP000001988; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0017038; P:protein import; IEA:InterPro.
DR   GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR   CDD; cd18803; SF2_C_secA; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_01382; SecA; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000185; SecA.
DR   InterPro; IPR020937; SecA_CS.
DR   InterPro; IPR011115; SecA_DEAD.
DR   InterPro; IPR014018; SecA_motor_DEAD.
DR   InterPro; IPR011130; SecA_preprotein_X-link_dom.
DR   InterPro; IPR044722; SecA_SF2_C.
DR   InterPro; IPR011116; SecA_Wing/Scaffold.
DR   InterPro; IPR036266; SecA_Wing/Scaffold_sf.
DR   InterPro; IPR036670; SecA_X-link_sf.
DR   PANTHER; PTHR30612; PTHR30612; 1.
DR   Pfam; PF07517; SecA_DEAD; 1.
DR   Pfam; PF01043; SecA_PP_bind; 1.
DR   Pfam; PF07516; SecA_SW; 1.
DR   PRINTS; PR00906; SECA.
DR   SMART; SM00957; SecA_DEAD; 1.
DR   SMART; SM00958; SecA_PP_bind; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF81767; SSF81767; 1.
DR   SUPFAM; SSF81886; SSF81886; 1.
DR   TIGRFAMs; TIGR00963; secA; 1.
DR   PROSITE; PS01312; SECA; 1.
DR   PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW   Protein transport; Translocase; Translocation; Transport.
FT   CHAIN           1..949
FT                   /note="Protein translocase subunit SecA 1"
FT                   /id="PRO_0000318389"
FT   REGION          869..949
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        924..938
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         86
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         104..108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         493
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   949 AA;  106022 MW;  D46C3315835E03D7 CRC64;
     MLSKLLRLGE GRMVKRLKKV ADYVGTLSDD VEKLTDAELR AKTDEFKRRL ADQKNPETLD
     DLLPEAFAVA REAAWRVLDQ RPFDVQVMGA AALHLGNVAE MKTGEGKTLT CVLPAYLNAL
     AGNGVHIVTV NDYLAKRDSE WMGRVHRFLG LQVGVILATM TPDERRVAYN ADITYGTNNE
     FGFDYLRDNM AHSLDDLVQR GHHYAIVDEV DSILIDEART PLIISGPADG ASNWYTEFAR
     LAPLMEKDVH YEVDLRKRTV GVHEKGVEFV EDQLGIDNLY EAANSPLVSY LNNALKAKEL
     FSRDKDYIVR DGEVLIVDEF TGRVLIGRRY NEGMHQAIEA KEHVEIKAEN QTLATITLQN
     YFRLYDKLAG MTGTAQTEAA ELHEIYKLGV VSIPTNMPMI REDQSDLIYK TEEAKYIAVV
     DDVAERYAKG QPVLIGTTSV ERSEYLSRQF TKRRIPHNVL NAKYHEQEAT IIAVAGRRGG
     VTVATNMAGR GTDIVLGGNV DFLTDQRLRE RGLDPVETPE EYEAAWHSEL PIVKEEASKE
     AKEVIEAGGL YVLGTERHES RRIDNQLRGR SGRQGDPGES RFYLSLGDEL MRRFNGAALE
     TLLTRLNLPD DVPIEAKMVT RAIKSAQTQV EQQNFEVRKN VLKYDEVMNQ QRKVIYAERR
     RILEGENLKD QALDMVRDVI TAYVDGATGE GYAEDWDLDA LWTALKTLYP VGITADSLTR
     KDHEFERDDL TREELLEALL KDAERAYAAR EAELEEIAGE GAMRQLERNV LLNVIDRKWR
     EHLYEMDYLK EGIGLRAMAQ RDPLVEYQRE GYDMFMAMLD GMKEESVGFL FNVTVEAVPA
     PPVAPAAEPA ELAEFAAAAA AAAQQRSAVD GGARERAPSA LRAKGVASES PALTYSGPAE
     DGSAQVQRNG GGAHKTPAGV PAGASRRERR EAARRQGRGA KPPKSVKKR